Analytical Data
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Gene name
VEGFA
- Application
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Alternative Names
VEGFA；VEGF；Vascular endothelial growth factor A. long form
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15692
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Expression Region
27-141aa
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AA Sequence
MAPMAEGGGQ NHHEVVKFMD VYQRSYCHPI ETLVDIFQEY PDEIEYIFKP SCVPLMRCGG CCNDEGLECV PTEESNITMQ IMRIKPHQGQ HIGEMSFLQH NKCECRPKKD RARQEKCDKP RR
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Molecular Weight
14 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Vascular endothelial growth factor A (VEGFA) is a crucial protein involved in angiogenesis, the process by which new blood vessels form from pre-existing ones. Its role in promoting endothelial cell proliferation, migration, and survival makes it a key player in various physiological and pathological conditions, including wound healing, tumorigenesis, and cardiovascular diseases. The overexpression of VEGFA is often associated with tumor progression as it stimulates angiogenesis, providing tumors with the necessary nutrients and oxygen for growth. Consequently, understanding VEGFA's mechanisms and interactions has become vital for developing therapeutic strategies against cancer and other diseases characterized by abnormal angiogenesis. Recent advancements in recombinant protein technology have allowed for the production of highly pure and active VEGFA, facilitating in-depth studies of its biological functions and interaction with receptors like VEGFR-1 and VEGFR-2. By utilizing these recombinant proteins, researchers can explore the pathways modulated by VEGFA, assess its potential as a biomarker for disease progression, and evaluate the efficacy of anti-angiogenic therapies. Furthermore, the ability to manipulate VEGFA levels in experimental models provides insights into the molecular mechanisms underlying its diverse roles in health and disease, paving the way for innovative treatment approaches that target VEGFA signaling in various angiogenesis-related conditions.
